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首页> 外文期刊>The Journal of Neuroscience: The Official Journal of the Society for Neuroscience >Association of beta 1 integrin with phosphotyrosine in growth cone filopodia.
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Association of beta 1 integrin with phosphotyrosine in growth cone filopodia.

机译：β1整合素与磷酸酪氨酸在生长锥体丝状伪足中的关联。

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Filopodia of growth cones are key elements in the transduction of extracellular cues that guide axon growth during development. How they are specialized to carry out this role is poorly understood. We previously had found tyrosine phosphorylated protein to be heavily concentrated at the tips of many filopodia of Aplysia growth cones in certain culturing conditions, suggesting that tyrosine phosphorylation might be involved in filopodial specialization. Immunocytochemistry was used to analyze the protein composition of the tip aggregates to determine whether there was an association of the tip phosphorylation with any important extracellular cue. beta 1 integrin, a subunit of the receptor for laminin-type neurite growth promoters, coconcentrated with phosphotyrosine at filopodial tips of both Aplysia and mouse growth cones. Several observations indicated that the association of beta 1 integrin with phosphotyrosine is close. beta 1 integrin and phosphotyrosine are known to colocalize at focal contacts, sites of adhesion of cells to the extracellular matrix, but the composition and behavior of the tip aggregates mark them as distinct structures. Also found in the tip aggregates was a member of the ezrin-radixin-moesin family of proteins, which are thought to link membrane proteins to submembranous bundles of actin filaments. Use of an inhibitor of protein-tyrosine kinases to deplete tip phosphotyrosine also caused disappearance of beta 1 integrin from the tip, suggesting a role for tyrosine phosphorylation in facilitating interaction of growth cones with certain environmental cues by fostering the aggregation of receptors in filopodia.
机译：生长锥的丝足是细胞外信号转导中的关键元素，细胞外信号在发育过程中指导轴突生长。人们对他们如何专门发挥这种作用知之甚少。我们以前发现酪氨酸磷酸化蛋白在某些培养条件下大量集中在海ly生长锥的许多丝状伪足的尖端，提示酪氨酸磷酸化可能参与了丝虫的专业化。免疫细胞化学用于分析尖端聚集体的蛋白质组成，以确定尖端磷酸化与任何重要的细胞外信号是否相关。 β1整联蛋白是层粘连蛋白型神经突生长促进剂受体的一个亚基，在海葵和小鼠生长锥的丝状末端与磷酸酪氨酸共同浓缩。一些观察结果表明，β1整联蛋白与磷酸酪氨酸的结合是紧密的。众所周知，β1整联蛋白和磷酸酪氨酸在局部接触处共定位，即细胞与细胞外基质的粘附部位，但是尖端聚集体的组成和行为将它们标记为不同的结构。在尖端聚集体中还发现了ezrin-radixin-moesin蛋白家族的成员，该蛋白被认为可将膜蛋白与肌动蛋白丝的亚膜束相连。使用蛋白质酪氨酸激酶抑制剂来耗尽尖端磷酸酪氨酸也可导致β1整联蛋白从尖端消失，这表明酪氨酸磷酸化通过促进丝状伪足中受体的聚集，在促进生长锥与某些环境线索的相互作用中起作用。

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